WASH4_HUMAN
ID WASH4_HUMAN Reviewed; 477 AA.
AC A8MWX3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Putative WAS protein family homolog 4;
DE AltName: Full=Protein FAM39CP;
GN Name=WASH4P; Synonyms=FAM39CP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [2]
RP GENE DUPLICATION.
RX PubMed=10655549; DOI=10.1093/hmg/9.3.395;
RA Ciccodicola A., D'Esposito M., Esposito T., Gianfrancesco F.,
RA Migliaccio C., Miano M.G., Matarazzo M.R., Vacca M., Franze A.,
RA Cuccurese M., Cocchia M., Curci A., Terracciano A., Torino A., Cocchia S.,
RA Mercadante G., Pannone E., Archidiacono N., Rocchi M., Schlessinger D.,
RA D'Urso M.;
RT "Differentially regulated and evolved genes in the fully sequenced Xq/Yq
RT pseudoautosomal region.";
RL Hum. Mol. Genet. 9:395-401(2000).
RN [3]
RP GENE DUPLICATION.
RX PubMed=18159949; DOI=10.1371/journal.pgen.0030237;
RA Linardopoulou E.V., Parghi S.S., Friedman C., Osborn G.E., Parkhurst S.M.,
RA Trask B.J.;
RT "Human subtelomeric WASH genes encode a new subclass of the WASP family.";
RL PLoS Genet. 3:E237-E237(2007).
CC -!- FUNCTION: May act as a nucleation-promoting factor at the surface of
CC endosomes, where it recruits and activates the Arp2/3 complex to induce
CC actin polymerization, playing a key role in the fission of tubules that
CC serve as transport intermediates during endosome sorting.
CC {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:C4AMC7}.
CC -!- SUBUNIT: Interacts (via WHD1 region) with WASHC2C; the interaction is
CC direct (By similarity). {ECO:0000250|UniProtKB:A8K0Z3}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:A8K0Z3}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q8VDD8}. Note=Localization to the endosome
CC membrane is mediated via its interaction with WASHC2.
CC {ECO:0000250|UniProtKB:A8K0Z3}.
CC -!- MISCELLANEOUS: WASH genes duplicated to multiple chromosomal ends
CC during primate evolution, with highest copy number reached in humans,
CC whose WASH repertoires probably vary extensively among individuals
CC (PubMed:18159949). It is therefore difficult to determine which gene is
CC functional or not. The telomeric region of chromosome 9p is paralogous
CC to the pericentromeric regions of chromosome 9 as well as to 2q.
CC Paralogous regions contain 7 transcriptional units. Duplicated WASH
CC genes are also present in the Xq/Yq pseudoautosomal region, as well as
CC on chromosome 1 and 15. The chromosome 16 copy seems to be a
CC pseudogene. {ECO:0000305|PubMed:18159949}.
CC -!- SIMILARITY: Belongs to the WASH1 family. {ECO:0000305}.
CC -!- CAUTION: The WASH4P N-terminus differs from WASH3P for which it is
CC shown to be required for the WASH complex assembly. Hence is
CC association within the WASH complex is ambiguous. However, WASH4P
CC retains the regions implicated in interaction with WASHC2 and confering
CC in vitro NPF activity. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; Z84812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A8MWX3; -.
DR SMR; A8MWX3; -.
DR ComplexPortal; CPX-1170; WASH complex, variant WASH4P/WASHC2C.
DR ComplexPortal; CPX-1175; WASH complex, variant WASH4P/WASHC2A.
DR IntAct; A8MWX3; 4.
DR STRING; 9606.ENSP00000317542; -.
DR iPTMnet; A8MWX3; -.
DR PhosphoSitePlus; A8MWX3; -.
DR BioMuta; HGNC:14126; -.
DR EPD; A8MWX3; -.
DR jPOST; A8MWX3; -.
DR MassIVE; A8MWX3; -.
DR MaxQB; A8MWX3; -.
DR PaxDb; A8MWX3; -.
DR PeptideAtlas; A8MWX3; -.
DR PRIDE; A8MWX3; -.
DR ProteomicsDB; 2275; -.
DR GeneCards; WASH4P; -.
DR HGNC; HGNC:14126; WASH4P.
DR neXtProt; NX_A8MWX3; -.
DR eggNOG; KOG1366; Eukaryota.
DR InParanoid; A8MWX3; -.
DR PhylomeDB; A8MWX3; -.
DR TreeFam; TF318222; -.
DR PathwayCommons; A8MWX3; -.
DR SignaLink; A8MWX3; -.
DR Pharos; A8MWX3; Tdark.
DR PRO; PR:A8MWX3; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; A8MWX3; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IC:ComplexPortal.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IC:ComplexPortal.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR InterPro; IPR028290; WASH1.
DR InterPro; IPR021854; WASH1_WAHD.
DR PANTHER; PTHR23331; PTHR23331; 1.
DR Pfam; PF11945; WASH_WAHD; 1.
PE 5: Uncertain;
KW Actin-binding; Endosome; Membrane; Reference proteome; Transport.
FT CHAIN 1..477
FT /note="Putative WAS protein family homolog 4"
FT /id="PRO_0000332291"
FT DOMAIN 374..396
FT /note="WH2"
FT REGION 1..180
FT /note="WHD1"
FT REGION 310..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..477
FT /note="VCA"
FT /evidence="ECO:0000250|UniProtKB:C4AMC7"
FT REGION 434..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..341
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 51595 MW; BBFD243389AC37A8 CRC64;
MSGVMCLKAS DTWASGIRSQ PQGCLGKWRS MRCKHTRMHL AHLGNSRQLI SLGPPRTRED
GSRISQQVEQ SRSQVQAIGE KVSLAQAKIE KIKGSKKAIK VFSSAKYPAP ERLQEYGSIF
TDAQDPGLQR RPRHRIQSKQ RPLDERALQE KLKDFPVCVS TKPEPEDDAE EGLGGLPSNI
SSVSSLLLFN TTENLYKKYV FLDPLAGAVT KTHVMLGAET EEKLFDAPLS ISKREQLEQQ
VPENYFYVPD LGQVPEIDVP SYLPDLPGIA NDLMYIADLG PGIAPSAPGT IPELPTFHTE
VAEPLKVDLQ DGVLTPPPPP PPPPPAPEVL ASAPPLPPST AAPVGQGARQ DDSSSSASPS
VQGAPREVVD PSGGWATLLE SIRQAGGIGK AKLRSMKERK LEKQQQKEQE QVRATSQGGH
LMSDLFNKLV MRRKGISGKG PGAGDGPGGA FARVSDSIPP LPPPQQPQAE DEDDWES
